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VPS25_RAT
ID   VPS25_RAT               Reviewed;         176 AA.
AC   P0C0A1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Vacuolar protein-sorting-associated protein 25;
DE   AltName: Full=ELL-associated protein of 20 kDa;
DE   AltName: Full=ESCRT-II complex subunit VPS25;
GN   Name=Vps25; Synonyms=Eap20;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 46-64; 110-117 AND 162-171, AND IDENTIFICATION IN A
RP   COMPLEX WITH ELL; SNF8 AND VPS36.
RC   TISSUE=Liver;
RX   PubMed=11278625; DOI=10.1074/jbc.m010142200;
RA   Kamura T., Burian D., Khalili H., Schmidt S.L., Sato S., Liu W.-J.,
RA   Conrad M.N., Conaway R.C., Conaway J.W., Shilatifard A.;
RT   "Cloning and characterization of ELL-associated proteins EAP45 and EAP20. a
RT   role for yeast EAP-like proteins in regulation of gene expression by
RT   glucose.";
RL   J. Biol. Chem. 276:16528-16533(2001).
CC   -!- FUNCTION: Component of the ESCRT-II complex (endosomal sorting complex
CC       required for transport II), which is required for multivesicular body
CC       (MVB) formation and sorting of endosomal cargo proteins into MVBs. The
CC       MVB pathway mediates delivery of transmembrane proteins into the lumen
CC       of the lysosome for degradation. The ESCRT-II complex is probably
CC       involved in the recruitment of the ESCRT-III complex (By similarity).
CC       The ESCRT-II complex may also play a role in transcription regulation,
CC       possibly via its interaction with ELL. {ECO:0000250}.
CC   -!- SUBUNIT: Component of a complex at least composed of ELL, SNF8/EAP30,
CC       VPS25/EAP20 and VPS36/EAP45 (By similarity). Component of the endosomal
CC       sorting complex required for transport II (ESCRT-II), composed of SNF8,
CC       VPS36 and 2 copies of VPS25. Interacts with CFTR; the interaction
CC       requires misfolded CFTR. Interacts (via C-terminal half) with the
CC       ESCRT-III subunit CHMP6 (via N-terminal half) (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome membrane
CC       {ECO:0000250}. Nucleus {ECO:0000250}. Note=Distributes diffusely
CC       throughout the cytoplasm and nucleoplasm, but exhibits a punctate
CC       distribution on coexpression with CHMP6. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the VPS25 family. {ECO:0000305}.
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DR   EMBL; AABR03074956; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CK471265; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; NP_001166922.1; NM_001173451.1.
DR   AlphaFoldDB; P0C0A1; -.
DR   SMR; P0C0A1; -.
DR   STRING; 10116.ENSRNOP00000044397; -.
DR   jPOST; P0C0A1; -.
DR   PRIDE; P0C0A1; -.
DR   GeneID; 681059; -.
DR   KEGG; rno:681059; -.
DR   CTD; 84313; -.
DR   RGD; 1584685; Vps25.
DR   VEuPathDB; HostDB:ENSRNOG00000020441; -.
DR   eggNOG; KOG4068; Eukaryota.
DR   HOGENOM; CLU_087657_0_1_1; -.
DR   OMA; SQEFHGM; -.
DR   OrthoDB; 1094121at2759; -.
DR   Reactome; R-RNO-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   PRO; PR:P0C0A1; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000051179; Expressed in spleen and 19 other tissues.
DR   Genevisible; P0C0A1; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0010008; C:endosome membrane; ISO:RGD.
DR   GO; GO:0000814; C:ESCRT II complex; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:RGD.
DR   GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR   GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; ISO:RGD.
DR   GO; GO:0043328; P:protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.10.570; -; 1.
DR   InterPro; IPR008570; ESCRT-II_cplx_Vps25-sub.
DR   InterPro; IPR014041; ESCRT-II_cplx_Vps25-sub_N.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR13149; PTHR13149; 1.
DR   Pfam; PF05871; ESCRT-II; 1.
DR   SUPFAM; SSF46785; SSF46785; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Endosome; Membrane; Nucleus;
KW   Protein transport; Reference proteome; Transcription;
KW   Transcription regulation; Transport.
FT   CHAIN           1..176
FT                   /note="Vacuolar protein-sorting-associated protein 25"
FT                   /id="PRO_0000215218"
FT   CONFLICT        53
FT                   /note="E -> Q (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   176 AA;  20762 MW;  AD4E3A4617BA4108 CRC64;
     MAMSFEWPWQ YRFPPFFTLQ PNVDTRQKQL AAWCSLVLSF CRLHKQSSMT VMEAQESPLF
     NNVKLQRKLP VESIQIVLEE LRKKGNLEWL DKNKSSFLIM WRRPEEWGKL IYQWVSRSGQ
     NNSVFTLYEL TSGEDTEEEE FHGLDEATLL RALQALQQEH KAEIITVSDG RGVKFF
 
 
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